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Membrane Protein Complexes (membrane + protein_complex)

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Life Sciences100%

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Cover Picture: Electrophoresis 12'2010

ELECTROPHORESIS, Issue 12 2010
Article first published online: 18 JUN 2010
Issue no. 12 is a regular issue comprising 19 contributions distributed over five distinct parts. Part I has 7 articles describing novel methodologies pertaining to proteins and proteomics. Part II has 3 research papers on CEC stationary phases and CEC-MS. Part III is on detection approaches including a review article on the advances and applications of chemiluminescence coupled to CE. Part IV has two papers on enantioseparations, and Part V has four contributions on aptamers, human genetic, preparative FFE and microchannels. Featured articles include: Simplified method for concentration of mitochondrial membrane protein complexes ((10.1002/elps.201000019)) Analysis of low-molecular mass aldehydes in drinking waters through capillary electrophoresis with laser-induced fluorescence detection ((10.1002/elps.200900734)) Selection of aptamers for signal transduction proteins by capillary electrophoresis ((10.1002/elps.200900543)) [source]

MicroCommentary: Subcellular localization of Escherichia coli osmosensory transporter ProP: focus on cardiolipin membrane domains

MOLECULAR MICROBIOLOGY, Issue 6 2007
Eugenia Mileykovskaya
Summary The role for specific lipids in the spatial distribution of the membrane proteins and formation of the lipid-protein membrane domains is an emerging theme in the studies of the supramolecular organization of the bacterial cell. A combination of the lipid and protein visualization techniques with manipulation of the cell lipid composition provides a useful tool for these studies. This MicroCommentary reviews the first experimental example demonstrating an involvement of the phospholipid cardiolipin in recruitment of a membrane protein (specifically H+ -osmoprotectant symporter ProP) to the Escherichia coli cell poles. The properties of cardiolipin domains employed in creating a specific environment for structural organization and function of membrane protein complexes are also discussed. [source]

Towards functional proteomics of membrane protein complexes: analysis of thylakoid membranes from Chlamydomonas reinhardtii

THE PLANT JOURNAL, Issue 5 2001
Michael Hippler
Summary Functional proteomics of membrane proteins is an important tool for the understanding of protein networks in biological membranes but structural studies on this part of the proteome are limited. In this study we undertook such an approach to analyse photosynthetic thylakoid membranes isolated from wild-type and mutant strains of Chlamydomonas reinhardtii. Thylakoid membrane proteins were separated by high-resolution two-dimensional gel electrophoresis (2-DE) and analysed by immuno-blotting and mass spectrometry for the presence of membrane-spanning proteins. Our data show that light-harvesting complex proteins (LHCP), that cross the membrane with three transmembrane domains, can be separated using this method. We have identified more than 30 different LHCP spots on our gels. Mass spectrometric analysis of 2-DE separated Lhcb1 indicates that this major LHCII protein can associate with the thylakoid membrane with part of its putative transit sequence. Separation of isolated photosystem I (PSI) complexes by 2-DE revealed the presence of 18 LHCI protein spots. The use of two peptide-specific antibodies directed against LHCI subunits supports the interpretation that some of these spots represent products arising from differential processing and post-translational modifications. In addition our data indicate that the reaction centre subunit of PSI, PsaA, that possesses 11 transmembrane domains, can be separated by 2-DE. Comparison between 2-DE maps from thylakoid membrane proteins isolated from a PSI-deficient (,ycf4) and a crd1 mutant, which is conditionally reduced in PSI and LHCI under copper-deficiency, showed the presence of most of the LHCI spots in the former but their absence in the latter. Our data demonstrate that (i) hydrophobic membrane proteins like the LHCPs can be faithfully separated by 2-DE, and (ii) that high-resolution 2-DE facilitates the comparative analysis of membrane protein complexes in wild-type and mutants cells. [source]